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P67870

- CSK2B_HUMAN

UniProt

P67870 - CSK2B_HUMAN

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Protein
Casein kinase II subunit beta
Gene
CSNK2B, CK2N, G5A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Participates in Wnt signaling By similarity. Plays a complex role in regulating the basal catalytic activity of the alpha subunit.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Zinc
Metal bindingi114 – 1141Zinc
Metal bindingi137 – 1371Zinc
Metal bindingi140 – 1401Zinc

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. protein domain specific binding Source: UniProtKB
  5. protein kinase regulator activity Source: UniProtKB
  6. receptor binding Source: BHF-UCL
  7. transcription factor binding Source: BHF-UCL

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. adiponectin-activated signaling pathway Source: BHF-UCL
  3. axon guidance Source: Reactome
  4. cellular protein complex assembly Source: BHF-UCL
  5. endothelial tube morphogenesis Source: BHF-UCL
  6. mitotic cell cycle Source: Reactome
  7. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  8. negative regulation of cell proliferation Source: BHF-UCL
  9. positive regulation of activin receptor signaling pathway Source: BHF-UCL
  10. positive regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  11. protein phosphorylation Source: GOC
  12. regulation of DNA binding Source: BHF-UCL
  13. regulation of protein kinase activity Source: GOC
  14. signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_150260. Condensation of Prometaphase Chromosomes.
REACT_200668. WNT mediated activation of DVL.
REACT_22272. Signal transduction by L1.
SignaLinkiP67870.

Names & Taxonomyi

Protein namesi
Recommended name:
Casein kinase II subunit beta
Short name:
CK II beta
Alternative name(s):
Phosvitin
Protein G5a
Gene namesi
Name:CSNK2B
Synonyms:CK2N, G5A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:2460. CSNK2B.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. nucleus Source: UniProtKB
  5. protein kinase CK2 complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 215214Casein kinase II subunit beta
PRO_0000068236Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine
Modified residuei2 – 21Phosphoserine; by autocatalysis1 Publication
Modified residuei3 – 31Phosphoserine; by autocatalysis1 Publication
Modified residuei209 – 2091Phosphoserine4 Publications
Modified residuei212 – 2121N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by alpha subunit.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP67870.
PaxDbiP67870.
PRIDEiP67870.

Expressioni

Gene expression databases

BgeeiP67870.
CleanExiHS_CSNK2B.
GenevestigatoriP67870.

Organism-specific databases

HPAiCAB004349.
CAB013087.
CAB016059.
HPA005944.

Interactioni

Subunit structurei

Tetramer composed of an alpha subunit, an alpha' subunit and two beta subunits. The beta subunit dimerization is mediated by zinc ions. Interacts with TCTEX1D3 By similarity. Interacts with CD163. Also component of a CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex associating following UV irradiation. Interacts with MUSK; mediates phosphorylation of MUSK by CK2. Interacts with FGF1; this interaction is increased in the presence of FIBP, suggesting a possible cooperative interaction between CSNKB and FIBP in binding to FGF1.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-348169,EBI-348169
CACNA1AO005552EBI-348169,EBI-766279
CBX4O00257-32EBI-348169,EBI-4392727
Clip1Q9JK252EBI-348169,EBI-908338From a different organism.
ClockO087852EBI-348169,EBI-79859From a different organism.
CSNK2A1P6840013EBI-348169,EBI-347804
CSNK2A2P197846EBI-348169,EBI-347451
PACS1Q6VY073EBI-348169,EBI-2555014
SIRT1Q96EB65EBI-348169,EBI-1802965

Protein-protein interaction databases

BioGridi107843. 210 interactions.
DIPiDIP-131N.
IntActiP67870. 178 interactions.
MINTiMINT-88683.
STRINGi9606.ENSP00000415615.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 157
Turni17 – 204
Helixi27 – 315
Helixi33 – 364
Helixi39 – 413
Beta strandi43 – 453
Helixi46 – 538
Beta strandi59 – 613
Helixi67 – 8721
Helixi91 – 10212
Turni103 – 1064
Helixi112 – 1143
Beta strandi120 – 1223
Beta strandi134 – 1363
Turni138 – 1403
Beta strandi142 – 1443
Helixi149 – 1513
Beta strandi152 – 1554
Helixi156 – 1583
Turni159 – 1624
Helixi163 – 1708
Helixi172 – 1743
Beta strandi187 – 1893
Beta strandi190 – 1923
Helixi195 – 1984
Turni199 – 2013
Helixi202 – 2054

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DS5X-ray3.16E/F/G/H181-203[»]
1JWHX-ray3.10C/D1-215[»]
1QF8X-ray1.74A/B1-182[»]
3EEDX-ray2.80A/B1-193[»]
4DGLX-ray3.00A/B1-215[»]
4MD7X-ray3.10A/B/C/D1-215[»]
4MD8X-ray3.30A/B/C/D1-215[»]
4MD9X-ray3.50A/B/C/D/I/J/N/O1-215[»]
4NH1X-ray3.30C/D1-215[»]
ProteinModelPortaliP67870.
SMRiP67870. Positions 7-207.

Miscellaneous databases

EvolutionaryTraceiP67870.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni188 – 1936Interaction with alpha subunit By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi55 – 6410Asp/Glu-rich (acidic)

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5041.
HOGENOMiHOG000039270.
HOVERGENiHBG051131.
InParanoidiP67870.
KOiK03115.
PhylomeDBiP67870.
TreeFamiTF314462.

Family and domain databases

Gene3Di1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.
InterProiIPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view]
PANTHERiPTHR11740. PTHR11740. 1 hit.
PfamiPF01214. CK_II_beta. 1 hit.
[Graphical view]
PRINTSiPR00472. CASNKINASEII.
SMARTiSM01085. CK_II_beta. 1 hit.
[Graphical view]
SUPFAMiSSF57798. SSF57798. 1 hit.
PROSITEiPS01101. CK2_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P67870-1 [UniParc]FASTAAdd to Basket

« Hide

MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL    50
DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK 100
YQQGDFGYCP RVYCENQPML PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR 150
HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ 200
LQAASNFKSP VKTIR 215
Length:215
Mass (Da):24,942
Last modified:October 11, 2004 - v1
Checksum:iE465B1E699B0E0EC
GO

Sequence cautioni

The sequence CAI18393.2 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti194 – 1941P → A in AAA52123. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16937 mRNA. Translation: CAA34811.1.
X16312 mRNA. Translation: CAA34379.1.
M30448 mRNA. Translation: AAA52123.1.
X57152 Genomic DNA. Translation: CAA40442.1.
AY113186 mRNA. Translation: AAM50092.1.
CR541699 mRNA. Translation: CAG46500.1.
AF129756 Genomic DNA. Translation: AAD18081.1.
BA000025 Genomic DNA. Translation: BAB63386.1.
DQ314868 Genomic DNA. Translation: ABC40727.1.
AK311860 mRNA. Translation: BAG34801.1.
AL662899 Genomic DNA. Translation: CAI96141.1.
AL662899 Genomic DNA. Translation: CAI18393.2. Different initiation.
AL670886 Genomic DNA. Translation: CAI17800.1.
AL805934 Genomic DNA. Translation: CAI18523.1.
BX511262 Genomic DNA. Translation: CAM45825.1.
CR753842 Genomic DNA. Translation: CAQ06572.1.
CR354443 Genomic DNA. Translation: CAQ07002.1.
CR759761 Genomic DNA. Translation: CAQ10879.1.
CH471081 Genomic DNA. Translation: EAX03473.1.
BC112017 mRNA. Translation: AAI12018.1.
BC112019 mRNA. Translation: AAI12020.1.
CCDSiCCDS4712.1.
PIRiA39459.
RefSeqiNP_001269314.1. NM_001282385.1.
NP_001311.3. NM_001320.6.
UniGeneiHs.73527.

Genome annotation databases

EnsembliENST00000375865; ENSP00000365025; ENSG00000204435.
ENST00000375866; ENSP00000365026; ENSG00000204435.
ENST00000375882; ENSP00000365042; ENSG00000204435.
ENST00000383427; ENSP00000372919; ENSG00000206406.
ENST00000383433; ENSP00000372925; ENSG00000206406.
ENST00000400110; ENSP00000382980; ENSG00000206406.
ENST00000412802; ENSP00000413469; ENSG00000224774.
ENST00000418230; ENSP00000411322; ENSG00000228875.
ENST00000422567; ENSP00000407018; ENSG00000224398.
ENST00000429633; ENSP00000409510; ENSG00000230700.
ENST00000431476; ENSP00000394855; ENSG00000224398.
ENST00000436169; ENSP00000412520; ENSG00000224398.
ENST00000443673; ENSP00000400188; ENSG00000230700.
ENST00000448596; ENSP00000391038; ENSG00000232960.
ENST00000451917; ENSP00000415303; ENSG00000224774.
ENST00000452985; ENSP00000415237; ENSG00000228875.
ENST00000453234; ENSP00000395275; ENSG00000224774.
ENST00000454382; ENSP00000390900; ENSG00000232960.
ENST00000454511; ENSP00000393756; ENSG00000232960.
ENST00000455161; ENSP00000407379; ENSG00000230700.
ENST00000458330; ENSP00000410802; ENSG00000228875.
GeneIDi1460.
KEGGihsa:1460.
UCSCiuc003nvr.1. human.

Polymorphism databases

DMDMi54037520.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16937 mRNA. Translation: CAA34811.1 .
X16312 mRNA. Translation: CAA34379.1 .
M30448 mRNA. Translation: AAA52123.1 .
X57152 Genomic DNA. Translation: CAA40442.1 .
AY113186 mRNA. Translation: AAM50092.1 .
CR541699 mRNA. Translation: CAG46500.1 .
AF129756 Genomic DNA. Translation: AAD18081.1 .
BA000025 Genomic DNA. Translation: BAB63386.1 .
DQ314868 Genomic DNA. Translation: ABC40727.1 .
AK311860 mRNA. Translation: BAG34801.1 .
AL662899 Genomic DNA. Translation: CAI96141.1 .
AL662899 Genomic DNA. Translation: CAI18393.2 . Different initiation.
AL670886 Genomic DNA. Translation: CAI17800.1 .
AL805934 Genomic DNA. Translation: CAI18523.1 .
BX511262 Genomic DNA. Translation: CAM45825.1 .
CR753842 Genomic DNA. Translation: CAQ06572.1 .
CR354443 Genomic DNA. Translation: CAQ07002.1 .
CR759761 Genomic DNA. Translation: CAQ10879.1 .
CH471081 Genomic DNA. Translation: EAX03473.1 .
BC112017 mRNA. Translation: AAI12018.1 .
BC112019 mRNA. Translation: AAI12020.1 .
CCDSi CCDS4712.1.
PIRi A39459.
RefSeqi NP_001269314.1. NM_001282385.1.
NP_001311.3. NM_001320.6.
UniGenei Hs.73527.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DS5 X-ray 3.16 E/F/G/H 181-203 [» ]
1JWH X-ray 3.10 C/D 1-215 [» ]
1QF8 X-ray 1.74 A/B 1-182 [» ]
3EED X-ray 2.80 A/B 1-193 [» ]
4DGL X-ray 3.00 A/B 1-215 [» ]
4MD7 X-ray 3.10 A/B/C/D 1-215 [» ]
4MD8 X-ray 3.30 A/B/C/D 1-215 [» ]
4MD9 X-ray 3.50 A/B/C/D/I/J/N/O 1-215 [» ]
4NH1 X-ray 3.30 C/D 1-215 [» ]
ProteinModelPortali P67870.
SMRi P67870. Positions 7-207.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107843. 210 interactions.
DIPi DIP-131N.
IntActi P67870. 178 interactions.
MINTi MINT-88683.
STRINGi 9606.ENSP00000415615.

Chemistry

BindingDBi P67870.
ChEMBLi CHEMBL2358.

Polymorphism databases

DMDMi 54037520.

Proteomic databases

MaxQBi P67870.
PaxDbi P67870.
PRIDEi P67870.

Protocols and materials databases

DNASUi 1460.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375865 ; ENSP00000365025 ; ENSG00000204435 .
ENST00000375866 ; ENSP00000365026 ; ENSG00000204435 .
ENST00000375882 ; ENSP00000365042 ; ENSG00000204435 .
ENST00000383427 ; ENSP00000372919 ; ENSG00000206406 .
ENST00000383433 ; ENSP00000372925 ; ENSG00000206406 .
ENST00000400110 ; ENSP00000382980 ; ENSG00000206406 .
ENST00000412802 ; ENSP00000413469 ; ENSG00000224774 .
ENST00000418230 ; ENSP00000411322 ; ENSG00000228875 .
ENST00000422567 ; ENSP00000407018 ; ENSG00000224398 .
ENST00000429633 ; ENSP00000409510 ; ENSG00000230700 .
ENST00000431476 ; ENSP00000394855 ; ENSG00000224398 .
ENST00000436169 ; ENSP00000412520 ; ENSG00000224398 .
ENST00000443673 ; ENSP00000400188 ; ENSG00000230700 .
ENST00000448596 ; ENSP00000391038 ; ENSG00000232960 .
ENST00000451917 ; ENSP00000415303 ; ENSG00000224774 .
ENST00000452985 ; ENSP00000415237 ; ENSG00000228875 .
ENST00000453234 ; ENSP00000395275 ; ENSG00000224774 .
ENST00000454382 ; ENSP00000390900 ; ENSG00000232960 .
ENST00000454511 ; ENSP00000393756 ; ENSG00000232960 .
ENST00000455161 ; ENSP00000407379 ; ENSG00000230700 .
ENST00000458330 ; ENSP00000410802 ; ENSG00000228875 .
GeneIDi 1460.
KEGGi hsa:1460.
UCSCi uc003nvr.1. human.

Organism-specific databases

CTDi 1460.
GeneCardsi GC06P031633.
GC06Pj31620.
GC06Pk31615.
GC06Pl31672.
GC06Pm31709.
GC06Pn31623.
GC06Po31622.
HGNCi HGNC:2460. CSNK2B.
HPAi CAB004349.
CAB013087.
CAB016059.
HPA005944.
MIMi 115441. gene.
neXtProti NX_P67870.
PharmGKBi PA26960.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5041.
HOGENOMi HOG000039270.
HOVERGENi HBG051131.
InParanoidi P67870.
KOi K03115.
PhylomeDBi P67870.
TreeFami TF314462.

Enzyme and pathway databases

Reactomei REACT_150260. Condensation of Prometaphase Chromosomes.
REACT_200668. WNT mediated activation of DVL.
REACT_22272. Signal transduction by L1.
SignaLinki P67870.

Miscellaneous databases

EvolutionaryTracei P67870.
GeneWikii CSNK2B.
GenomeRNAii 1460.
NextBioi 6001.
PROi P67870.
SOURCEi Search...

Gene expression databases

Bgeei P67870.
CleanExi HS_CSNK2B.
Genevestigatori P67870.

Family and domain databases

Gene3Di 1.10.1820.10. 1 hit.
2.20.25.20. 1 hit.
InterProi IPR016149. Casein_kin_II_reg-sub_a-hlx.
IPR016150. Casein_kin_II_reg-sub_b-sht.
IPR000704. Casein_kinase_II_reg-sub.
[Graphical view ]
PANTHERi PTHR11740. PTHR11740. 1 hit.
Pfami PF01214. CK_II_beta. 1 hit.
[Graphical view ]
PRINTSi PR00472. CASNKINASEII.
SMARTi SM01085. CK_II_beta. 1 hit.
[Graphical view ]
SUPFAMi SSF57798. SSF57798. 1 hit.
PROSITEi PS01101. CK2_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human phosvitin/casein kinase type II. Molecular cloning and sequencing of full-length cDNA encoding subunit beta."
    Jakobi R., Voss H., Pyerin W.
    Eur. J. Biochem. 183:227-233(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expression of the cDNA for the beta subunit of human casein kinase II confers partial UV resistance on xeroderma pigmentosum cells."
    Teitz T., Eli D., Penner M., Bakhanashvili M., Naiman T., Timme T.L., Wood C.M., Moses R.E., Canaani D.
    Mutat. Res. 236:85-97(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and characterization of a cDNA encoding the beta subunit of human casein kinase II."
    Heller-Harrison R.A., Meisner H., Czech M.P.
    Biochemistry 28:9053-9058(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Structure of the gene encoding human casein kinase II subunit beta."
    Voss A., Wirkner U., Jacobi R., Hewitt N., Schwager C., Zimmermann J., Ansorge W., Pyerin W.
    J. Biol. Chem. 266:13706-13711(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Sequencing of full-length cDNA encoding the alpha and beta subunits of human casein kinase II from human platelets and megakaryocytic cells. Expression of the casein kinase IIalpha intronless gene in a megakaryocytic cell line."
    Singh L.S., Kalafatis M.
    Biochemistry 41:8935-8940(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
    Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
    Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
    Shiina S., Tamiya G., Oka A., Inoko H.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  10. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  14. "Stimulation of casein kinase II by epidermal growth factor: relationship between the physiological activity of the kinase and the phosphorylation state of its beta subunit."
    Ackerman P., Glover C.V., Osheroff N.
    Proc. Natl. Acad. Sci. U.S.A. 87:821-825(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  15. "Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C."
    Ritter M., Buechler C., Kapinsky M., Schmitz G.
    Eur. J. Immunol. 31:999-1009(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CD163.
  16. "A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1."
    Keller D.M., Zeng X., Wang Y., Zhang Q.H., Kapoor M., Shu H., Goodman R., Lozano G., Zhao Y., Lu H.
    Mol. Cell 7:283-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H.
  17. "Identification of ribosome-binding protein p34 as an intracellular protein that binds acidic fibroblast growth factor."
    Skjerpen C.S., Wesche J., Olsnes S.
    J. Biol. Chem. 277:23864-23871(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGF1.
  18. "p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex."
    Keller D.M., Lu H.
    J. Biol. Chem. 277:50206-50213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSRP1 AND SUPT16H.
  19. "Casein kinase 2-dependent serine phosphorylation of MuSK regulates acetylcholine receptor aggregation at the neuromuscular junction."
    Cheusova T., Khan M.A., Schubert S.W., Gavin A.C., Buchou T., Jacob G., Sticht H., Allende J., Boldyreff B., Brenner H.R., Hashemolhosseini S.
    Genes Dev. 20:1800-1816(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MUSK, INTERACTION WITH MUSK.
  20. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "Crystal structure of the human protein kinase CK2 regulatory subunit reveals its zinc finger-mediated dimerization."
    Chantalat L., Leroy D., Filhol O., Nueda A., Benitez M.J., Chambaz E.M., Cochet C., Dideberg O.
    EMBO J. 18:2930-2940(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 1-182, SUBUNIT, ZINC-BINDING SITES.
  28. "Crystal structure of human protein kinase CK2: insights into basic properties of the CK2 holoenzyme."
    Niefind K., Guerra B., Ermakowa I., Issinger O.G.
    EMBO J. 20:5320-5331(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CSNK2A1, ZINC-BINDING SITES, SUBUNIT, PHOSPHORYLATION AT SER-2 AND SER-3.

Entry informationi

Entry nameiCSK2B_HUMAN
AccessioniPrimary (citable) accession number: P67870
Secondary accession number(s): B0UXA9
, P07312, P13862, Q4VX47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: September 3, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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